Chapter # 01

BIOMOLECULE
BIOCHEMISRTY
The branch of biology which deals with the study of chemical basis of life is called biochemistry.
Importance
Biochemistry provides us knowledge about all the chemical reactions e.g. protein synthesis, photosynthesis,
respiration, etc which are going on every instant in bodies of living organisms.
It has played a major part in the improvement of health by the manufacture
of a number of drugs. In plants usage of pesticides and fertilizers has reduced
the diseases a lot.
As a whole, biochemistry is the base of biology in modern ages.
BIOCHEMISTRY: “The branch of biology which deals with the biochemical
basis of life is called biochemistry”.
Chemical Composition Cell.
• Living material of cell called Protoplasm, It contain 70-90% water
• The compounds which are formed by the living organism are called
biological molecules. (Biochemicals)
Contribution of Elements in Biochemistry:
• Only six elements CARBON (C), HYDROGEN (H), NITROGEN (N), OXYGEN
(O), PHOSPHORUS (P) and SULPHUR (S) make up most (about 98%) of
biochemicals.
ORGANIC COMPOUNDS
• Those compounds containing carbon with hydrogen are called organic compounds.
• E.g. CARBOHYDRATES, PROTEINS, LIPIDS AND NUCLEIC ACID.
MACROMOLECULES (Macro = large) means “giant molecule.”
• Monomers (Mono = single; mer = part) are small molecules which are joined together to produce large
compounds.
• Polymers (Poly = many; mer = part) are large compounds formed by the joining of smaller units of monomers.
• The monomers may be identical, or they may be different.
• CONDENSATION: The process by which two monomers are joined is called “Condensation”. Also called
“Dehydration Synthesis” because water is removed (dehydration ) and a bond is made (synthesis).
• HYDROLYSIS: A process during which polymers are broken down into their subunits (monomers) by the
addition of H2O called “Hydrolysis”. It is just reverse of the condensation.

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WATER: “Hydrogen oxide”
• It amount varies from 70-90%. It is polar molecules.
• It has slightly –ve end the oxygen atom and slightly +ve end the Hydrogen atom.
• The electrical charge separation of water molecules is called Dipole .
Biologically Important Properties of Water:
1. Universal solvent
2. High Heat Capacity
3. High Heat of Vaporization
4. An Amphoteric Molecules
5. As a Buffer Molecule
6. Cohesive force
▪ UNIVERSAL SOLVENT: Because it is charged, water is a very good solvent.
▪ Charged or polar molecules such as salts, sugars and amino acids dissolve readily in water and so are
called hydrophilic ("water loving").
▪ Uncharged or non-polar molecules such as lipids do not dissolve so well in water and are
called hydrophobic ("water hating").
▪ SPECIFIC HEAT CAPACITY: Water has a specific heat capacity of 4.2 J g-1 °C-1, which means that it takes 4.2 joules
of energy to heat 1 g of water by 1°C.
▪ This is unusually high and it means that water does not change temperature very easily.
▪ This minimizes fluctuations in temperature inside cells, and it also means that sea temperature is remarkably
constant.
▪ LATENT HEAT OF EVAPORATION: Water requires a lot of energy to change state from a liquid into a gas, and
this is made use of as a cooling mechanism in animals (sweating and panting) and plants (transpiration).
▪ As water evaporates it extracts heat from around it, cooling the organism.
▪ DENSITY: (Anomalous behavior) Water is unique in that the solid state (ice) is less dense that the liquid state,
so ice floats on water.
▪ As the air temperature cools, bodies of water freeze from the surface, forming a layer of ice with liquid water
underneath. This allows aquatic ecosystems to exist even in sub-zero temperatures.
▪ COHESION/ADHESION: Water molecules "stick together" due to their hydrogen bonds, so water has high
cohesion. This explains why long columns of water can be sucked up tall trees by transpiration without breaking.
▪ It also explains surface tension, which allows small animals to walk on water.
▪ IONIZATION: When many salts dissolve in water they ionize into discrete
positive and negative ions (e.g. NaCl Na+ + Cl-).
▪ Many important biological molecules are weak acids, which also ionize in
solution (e.g. acetic acid acetate- + H+).
▪ pH: Water itself is partly ionized (H2O H+ + OH- ), so it is a source of protons
(H+ ions), and indeed many biochemical reactions are sensitive to pH (-log[H+]).
▪ AN AMPHOTERIC MOLECULE:
▪ Pure water cannot buffer changes in H+ concentration, so is not a buffer and can easily be any pH, but the
cytoplasm and tissue fluids of living organisms are usually well buffered at about neutral pH (pH 7-8).

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1. CARBOHYDRATES: Carbo = Carbon, Hydrate = Water
▪ Carbohydrates are a group of naturally occurring carbonyl compounds (aldehydes or ketones) that also
contain several hydroxyl groups.
▪ They are the most abundant organic molecules in nature and are also referred to as “saccharides”.
▪ The carbohydrates which are soluble in water
and sweet in taste are called “sugars”.
▪ Structure of Carbohydrates
▪ Carbohydrates consist of C, H, and O
▪ The general empirical structure for
carbohydrates is (CH2O) n.
▪ Ratio of hydrogen and oxygen is same as in
water. (2:1) so called “Hydrated Carbon”
▪ They are organic compounds organized in the form of aldehydes or ketones with multiple hydroxyl groups
coming off the carbon chain.
▪ The building blocks of all carbohydrates are simple sugars called monosaccharides.
▪ A monosaccharide can be a polyhydroxy aldehyde (aldose) or a polyhydroxy ketone (ketose).
▪ MONOSACCHARIDES
▪ The simplest group of carbohydrates and often called simple sugars since they cannot be further hydrolyzed.
▪ Colorless, crystalline solids that are soluble in water. with sweet taste
▪ These are compound that possesses a free aldehyde or ketone group.
▪ The general formula is CnH2nOn.
▪ Examples: Glucose, Fructose, Ribulose.
▪ Isomers
▪ Glucose & fructose are isomers b/c their
structures are different, but their chemical
formulas are the same.
▪ OLIGOSACCHARIDES
▪ Oligosaccharides are compound sugars that yield 2 to 10 molecules of the same or different monosaccharides
on hydrolysis.
▪ The monosaccharide units are joined by glycosidic linkage.
▪ Based on the number of monosaccharide units, it is further
classified as a disaccharide, trisaccharide, tetrasaccharide, etc.
▪ Oligosaccharides yielding 2 molecules of monosaccharides on
hydrolysis is known as a disaccharide.
▪ Examples: Disaccharides include sucrose, lactose, maltose, etc.
▪ Maltose occurs to a limited extent in sprouting grain. It is
formed most often by the partial hydrolysis of starch and glycogen.
In the manufacture of beer, maltose is liberated by the action of malt (germinating barley) on starch; for this reason,
it is often referred to as malt sugar.
▪ Lactose is known as milk sugar because it occurs in the milk of humans, cows, and other mammals.
▪ Sucrose, probably the largest-selling pure organic compound in the world, is known as beet sugar, cane
sugar, table sugar, or simply sugar. Most of the sucrose sold commercially is obtained from sugar cane and sugar
beets

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▪ POLYSACCHARIDES
▪ They are also called “glycans”.
▪ Polysaccharides contain more than 10 monosaccharide units
▪ They are primarily concerned with two important functions ie. Structural functions and the storage of energy.
▪ They are further classified depending on the type of molecules produced as a result of hydrolysis.
▪ They may be homopolysaccharides, containing monosaccharides of the same type
or heteropolysaccharides i.e., monosaccharides of different types.
▪ Examples of Homopolysaccharides are starch, glycogen, cellulose, pectin.
▪ Heteropolysaccharides are Hyaluronic acid, Chondroitin.
▪ STARCH
▪ Starch is the most important source of
carbohydrates in the human diet and
accounts for more than 50% of our
carbohydrate intake.
▪ It occurs in plants in the form of
granules, and these are particularly
abundant in seeds (especially the cereal grains) and tubers, where they serve as a storage form of carbohydrates.
▪ Starch is a mixture of two polymers: amylose and amylopectin. Natural starches consist of about 10%–30%
amylase and 70%–90% amylopectin.
▪ Amylose is a linear polysaccharide; Amylopectin is a branched-chain polysaccharide composed of glucose units.
▪ The characteristic blue-violet color that appears when starch is treated with iodine.
▪ GLYCOGEN
▪ Glycogen is the energy reserve carbohydrate of animals. Glycogen is structurally quite similar to amylopectin,
although glycogen is more highly branched (8–12 glucose units between branches) and the branches are shorter.
When treated with iodine, glycogen gives a reddish-brown color.
▪ CELLULOSE
▪ Cellulose, a fibrous carbohydrate found in all plants, is the
structural component of plant cell walls. Because the earth is covered
with vegetation, cellulose is the most abundant of all carbohydrates,
▪ Like amylose, cellulose is a linear polymer of glucose.
▪ It does not bind to iodine to form a colored product.
▪ CHITIN another structural polysaccharide, is found in the
exoskeleton of arthropods.
▪ Chitin also provides structural support for the cell walls of fungi.
▪ Unlike starch and glycogen, chitin is a polysaccharide with
nitrogen (N) in each sugar monomer.
▪ FUNCTIONS OF CARBOHYDRATES
▪ Regular source of energy
▪ Stored source of energy
▪ Building, protective & supporting structure
▪ They make cell wall
▪ Make exoskeleton in arthropods.

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2. PROTEINS (Gr: Proteios means “First Rank”)
• Proteins are most important organic compounds. Side chain (R group)

• They carry out all activities of the cell  Carbon

• They constitute more than 50% of dry weight
• Proteins contain C, H, O and N. but sometimes P and S also.
• The name Protein was suggested by Berzelius in 1838.
• G.J.Murlder in 1883 recognized the importance of protein.
Amino group Carboxyl group
• Building Blocks of Proteins:
• Amino acids are the building block joined together by peptide bonding.
• There are 20 different amino acids. The order of amino acids in a protein is important.
• The amino acids differ on the nature of the R group. Examples of amino acids are:
• Valine, Alanine, Glutamic acid, Tyrosine and Histidine.
• PEPTIDE LINKAGE
• In addition to its R group, each amino acid, when ionized, has a
positive amino (NH3 +) group at one end and a negative carboxyl
(COO– ) group at the other.
• The amino and carboxyl groups on a pair of amino acids can
undergo a dehydration reaction to form a covalent bond.
• The covalent bond that links two amino acids is called a peptide
bond.
Structure of Proteins: There are four basic levels of proteins.
1. Primary Structure A linear sequence of amino-acids. E.g. Insulin
2. Secondary Structure Chain of amino-acids become spirally coiled. results in the formation of a rigid and tubular
structure called “Helix”. The hydrogen and sulphide bonds are involved to hold the protein chain in spiral manner.
E.g. hairs, spider’s webs.
3. Tertiary Structure Polypeptide chain bends and folds upon
it self forming a globular shape. It is maintained by three types
of bonds. Namely ionic, hydrogen and disulphide (S-S). E.g.
Lysozyme
4. Quaternary Structure This type is usually present in highly
complex proteins in which polypeptide tertiary chains are
aggregated and held together by hydrophobic interactions,
hydrogen and ionic bonds. E.g. Hemoglobin molecule.
• INSULIN STRUCTURE
• It has two long amino acid chains or polypeptide chains.
The chains are chain A with 21 amino acids and chain B with
30 amino acids.
• Two disulfide bonds (residues A7 to B7, and A20 to B19)
covalently connect the chains, and chain A contains an internal
disulfide bond (residues A6 to A11).

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• Classification on the basis of shape
• Fibrous protein (Scleroprotein):
• We can find these proteins in animals and are insoluble in water.
• Fibrous proteins are resistant to proteolytic enzymes and are coiled and exist in threadlike structures to form
fibres.
• e.g. collagen, actin, and myosin, keratin in hair, claws, feathers, etc.
• Globular proteins:
• These proteins, unlike fibrous proteins are soluble in water.
• They are made up of polypeptides that are coiled about themselves to form oval or spherical molecules.
• e.g. albumin, insulin, and hormones like oxytocin, etc.
• FUNCTIONS OF PROTEINS:
• Functional classification of proteins Based on the functions they perform, proteins are classified into the
following groups (with examples)
1. Structural proteins: Keratin of hair and nails, collagen of bone. 2. Enzymes or catalytic proteins: Hexokinase,
pepsin. 3. Transport proteins: Hemoglobin, serum albumin. 4. Hormonal proteins: Insulin, growth hormone. 5.
Contractile proteins: Actin, myosin. 6. Storage proteins: Ovalbumin, glutelin. 7. Genetic proteins: Nucleoproteins.
8. Defense proteins: Snake venoms, Immunoglobulins. 9. Receptor proteins: for hormones, viruses
3. LIPIDS:
▪ Important diverse group of biomolecules widely distributed among plants and animals. Bloor (1943) used term
lipid. (Organic compounds) containing C, H and O like carbohydrates.
▪ Oxygen is much less C57 H104O6, Insoluble in water & soluble in organic solvent. Following are the important
groups of Lipids.
▪ i. Acylglycerol (fats & oils) ii. Waxes
▪ iii. Phospholipids iv. Terpenoids (Terpens, Steroids & Carotenoids)
▪ ACYLGLYCEROL (FATS AND OIL)
▪ Found in plants and animals
▪ Rich in energy supply (over double)
▪ 16 Kg fat/person (144000 K cal)
▪ They are made when 3 fatty acids condense with 1 glycerol molecule
▪ They are also called TRIGLYCERIDE
a. Saturated acylglycerol b. Unsaturated acylglycerol
Contain saturated fatty acids Contain unsaturated fatty acids
Don't contain double bond b/w C atom. Contain 1 or more double bond b/w C atom
Solid at ordinary temp: Liquid at ordinary temp:
Mostly found in animals called FAT Found in plants and are called OIL
E.g. Stearin found in BEEF and MUTTON E.g. Lanolin in cotton seed
Waxes:
▪ They are simple lipids & water repellent and not – reactive.
▪ One molecule of fatty acids makes Easter bond with one molecule of alcohol
▪ Found as protective covering on fruits, leaves, skin, fur etc.
▪ E.g. Bee’s Wax

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Phospholipids:
▪ They are similar to triacylglycerol or oil except one fatty
acid is replaced by phosphate group.
▪ They are wide spread in bacteria, animal and plant cell
frequently associated with membranes.
▪ 2 molecules of fatty acids + one molecule of phosphate
are required
▪ Head is water soluble (Hydrophilic)
▪ Tail is water insoluble (Hydrophobic)
Terpenoids:
▪ It is large class of lipids E.g. Steroids, Carotenoids and Terpens
▪ They are buildup of isoprenoid (C5 H8) units.
▪ Steroids, carotenoids and terpenes are important classes of it.
▪ They provide insulation, mechanical support and protection from water loss.
TERPENES
▪ Small size - Volatile in nature - Produce special fragrance - Used in perfumes
▪ E.g. Limonene (Lemon), Mycerene (oil of bay), Geranoil (Rose) Menthol (Peppermint) etc.
▪ Also found in Vitamin A1 and A2 - They are present in chlorophyll
▪ Their main use is in RUBBER and LATEX formation
STEROIDS
▪ They consist of three 6 membered and one 5 membered carbon rings.
▪ E.g. Cholesterol which is found in cell membrane, sex hormones
(Testosterone, Progesteron, Estrogen)
CAROTENOIDS
▪ Made up of fatty acid like carbon chain
▪ They are present in Carotene and xanthophylls which produce Red, Orange, Cream, and Brown colors in plants
Functions of lipids:
Long term energy storage (fuel reserve of the body (triacylglycerols). Source of fat-soluble vitamins (A, D, E and K).
Protection against heat loss (insulation). Protection against physical shock. Protection against water loss. Chemical
messengers (Steroid hormones and prostaglandins). Major component of membranes (phospholipids)
4. NUCLEIC ACIDS:
▪ DNA and RNA are two types of Nucleic Acids. Nucleic acids contain C, H, O, N and P.
▪ They are complex substances polymers of nucleotides. These were Isolated by F. Miescher in 1870.
▪ These are present from VIRUS to MAN. DNA is found in cell nucleus & 90% RNA is found in cytoplasm
▪ Nucleotide consist of three parts (i) Pentose sugar (ii) Phosphoric acid (H3 PO4) (iii) A nitrogenous base
▪ Pentose sugar is either Ribose (C5H10O5) or Deoxyribose (C5H10O4)
▪ Phosphoric acid is common in all nucleotides
▪ Nitrogenous Bases are of two types (i)Purine (A – G) (ii) Pyrimidine (C – T – U)
▪ All these bases are similar in DNA and RNA except thymine is present in DNA while Uracil in RNA.

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▪ Formation of Nucleotide: Takes place in two steps: -
▪ In first step Nucleoside is formed when nitrogenous bases combine
with pentose sugar.
▪ In the 2nd step nucleotide is formed when phosphoric acid
combines with fifth carbon of the pentose sugar.
MONONUCLEOTIDE:
• Nucleotides are also found in the form of mononucleotide or
dinucleotide
• These exist singly or part of another molecule
• These are not the part of DNA or RNA e.g. ATP.
• Role of ATP as energy currency:
• ATP is currency note. It gives energy to all cells
• It is basically made from carbohydrates. ATP is composed of:
• i. Adenine ii. Ribose sugar iii. 3 Phosphates
• It produces 7.3 K cal/ mole or 31.81 KJ /mole energy
• ATP receive energy from one reaction and transfer it to
another reaction in body
DINCULEOTIDES:
• These nucleotides are covalently bounded together and usually act as co-enzymes. E.g. NAD (Nicotinamide
adenine dinucleotide).
POLYNUCLEOTIDES:
• Nucleotides are found in the nucleic acid as “Polynucleotide” and they have a variety of role in living organisms.
• They usually perform the function of transmitters of genetic information. E.g. DNA and RNA
WATSON AND CRICK'S MODEL OF DNA
James Watson and Francis Crick, in 1953 proposed structure of the DNA molecule.
Structure of DNA: Watson and Crick suggested a ladder like organization of DNA.
i. Double Helix ii. Backbone of DNA iii. Pairing of Bases
i. Double Helix: Each molecule of DNA is made up of two polynucleotide chains which twisted around each other
and form a double helix.
ii. Backbone of DNA: The uprights of the ladder are made up of sugar and phosphate parts of nucleotide and the
rungs are made up of a paired nitrogenous base.
iii. Pairing of Bases: The pairs are always as follows
• Adenine always pairs with thymine and cytosine with Guanine.
• The two polynucleotide chains are complimentary to each other and held together by hydrogen bonds.
Hydrogen Bonding: There are two hydrogen bonds between Adenine and Thymine (A=T) and three between
Cytosine and Guanine.
Distance
• Both polynucleotide strands remain separated by 20 A° distance.
• The coiling of double helix is right-handed and complete turn occurs after 3.4 A°. In each turn 10 nucleotide
pairs are present; therefore, the distance between two pairs is about 3.4 A°.

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RNA (As a carrier of information):
▪ Eukaryotic DNA is located in the nucleus
▪ Most of synthesis, Metabolic function occur in the cytoplasm.
▪ This synthesis Metabolic function are carried out under the instruction of DNA
▪ Information from DNA to cytoplasm are carried by RNA
Types of RNA: There are three types of RNA.
▪ Ribosomal RNA (rRNA): The class of RNA found in ribosome is called ribosomal RNA.
Function: During polypeptide synthesis it provides the site on the ribosome where the polypeptide is assembled.
▪ Transfer RNA (tRNA): A second class of RNA is called transfer RNA is much smaller. Human cell contains more
than 40 different kinds of tRNA molecules.
Function: During polypeptide synthesis tRNA
molecules transport the amino acid into the ribosome
for the synthesis of polypeptide chain.
▪ Messenger RNA (mRNA): It is long strand of RNA
that passes from the nucleus to the Cytoplasm.
▪ Function: During polypeptide synthesis, mRNA
molecules bring information from the chromosomes to
the ribosome to direct the assembly of amino acids into
a polypeptide.
▪ (i)Transcription: In this step information flow from
DNA to m- RNA by DNA copying.
▪ (ii)Translation: In this step t-RNA and specific RNA
translate specific sequence of Amino acid which help to synthesize proteins.
CONJUGATED MOLECULES:
• Two different biomolecules belonging to different categories are called conjugated molecules. There are four
different types of conjugated molecules.
• Glycolipids: Lipids + Carbohydrates Glycolipids
• Glycoproteins: Protein + Carbohydrates Glycoprotein
• Nucleoprotein: Protein + Nucleic acid Nucleoproteins.
• Lipoproteins: Protein + Lipid Lipoproteins.

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